LIN10_CAEEL
ID LIN10_CAEEL Reviewed; 982 AA.
AC O17583; Q9XZQ5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein lin-10;
DE AltName: Full=Abnormal cell lineage protein 10;
GN Name=lin-10 {ECO:0000312|WormBase:C09H6.2a};
GN ORFNames=C09H6.2 {ECO:0000312|WormBase:C09H6.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=10359617; DOI=10.1091/mbc.10.6.2087;
RA Whitfield C.W., Benard C., Barnes T., Hekimi S., Kim S.K.;
RT "Basolateral localization of the Caenorhabditis elegans epidermal growth
RT factor receptor in epithelial cells by the PDZ protein lin-10.";
RL Mol. Biol. Cell 10:2087-2100(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=2159938; DOI=10.1101/gad.4.3.357;
RA Kim S.K., Horvitz H.R.;
RT "The Caenorhabditis elegans gene lin-10 is broadly expressed while required
RT specifically for the determination of vulval cell fates.";
RL Genes Dev. 4:357-371(1990).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-15;
RP THR-26; THR-28; SER-87; SER-155; SER-201; THR-358; THR-424; THR-444 AND
RP SER-448.
RX PubMed=17671168; DOI=10.1091/mbc.e06-09-0818;
RA Juo P., Harbaugh T., Garriga G., Kaplan J.M.;
RT "CDK-5 regulates the abundance of GLR-1 glutamate receptors in the ventral
RT cord of Caenorhabditis elegans.";
RL Mol. Biol. Cell 18:3883-3893(2007).
RN [5]
RP FUNCTION, INTERACTION WITH EGL-9, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP HYDROXYLATION, AND MUTAGENESIS OF SER-15; PRO-16; THR-26; PRO-27; THR-28;
RP PRO-29; SER-87; PRO-88; SER-155; PRO-156; SER-201; PRO-202; THR-358;
RP PRO-359; THR-424; PRO-425; THR-444; PRO-445; SER-448 AND PRO-449.
RX PubMed=22252129; DOI=10.1038/emboj.2011.499;
RA Park E.C., Ghose P., Shao Z., Ye Q., Kang L., Xu X.Z., Powell-Coffman J.A.,
RA Rongo C.;
RT "Hypoxia regulates glutamate receptor trafficking through an HIF-
RT independent mechanism.";
RL EMBO J. 31:1379-1393(2012).
RN [6]
RP FUNCTION, INTERACTION WITH RAB-6.2, AND SUBCELLULAR LOCATION.
RX PubMed=22213799; DOI=10.1083/jcb.201104141;
RA Zhang D., Isack N.R., Glodowski D.R., Liu J., Chen C.C., Xu X.Z.,
RA Grant B.D., Rongo C.;
RT "RAB-6.2 and the retromer regulate glutamate receptor recycling through a
RT retrograde pathway.";
RL J. Cell Biol. 196:85-101(2012).
CC -!- FUNCTION: Required specifically for the determination of 3 vulval
CC precursor cell fates P5.p, P6.p and P7.p during late second and early
CC third larval stages; required for basolateral localization of receptor
CC tyrosine kinase let-23. Could have a general but redundant role in
CC development, functioning in diverse cell lineages to control cell fates
CC (PubMed:10359617, PubMed:2159938). Regulates the trafficking of the
CC glr-1 subunit of AMPA-type glutamate receptors (AMPRs) in the ventral
CC nerve cord (PubMed:17671168, PubMed:22252129, PubMed:22213799). This
CC may be partly through interacting with the small GTPase rab-6.2 in its
CC active GTP-bound state (PubMed:22213799). {ECO:0000269|PubMed:10359617,
CC ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:2159938,
CC ECO:0000269|PubMed:22213799, ECO:0000269|PubMed:22252129}.
CC -!- SUBUNIT: Interacts (via N-terminus) with egl-9 isoform e (via catalytic
CC domain); the interaction regulates its trafficking; the interaction is
CC direct (PubMed:22252129). Interacts with rab-6.2 (in GTP-bound form)
CC (PubMed:22213799). {ECO:0000269|PubMed:22213799,
CC ECO:0000269|PubMed:22252129}.
CC -!- INTERACTION:
CC O17583; Q19955: ags-3; NbExp=2; IntAct=EBI-313389, EBI-2913838;
CC O17583; O01427: air-2; NbExp=2; IntAct=EBI-313389, EBI-312947;
CC O17583; O45952: csc-1; NbExp=2; IntAct=EBI-313389, EBI-328477;
CC O17583; P54936: lin-2; NbExp=5; IntAct=EBI-313389, EBI-315019;
CC O17583; G5EC32: sorb-1; NbExp=6; IntAct=EBI-313389, EBI-325337;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:10359617}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10359617}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:10359617}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10359617}. Cytoplasm {ECO:0000269|PubMed:22252129}.
CC Synapse {ECO:0000269|PubMed:17671168}. Perikaryon
CC {ECO:0000269|PubMed:22213799}. Note=In trans cisternae of Golgi or
CC trans-Golgi network (PubMed:10359617). Localizes to Gogli-associated
CC structures (PubMed:22213799). Partially co-localizes with glr-1 at the
CC synapse (PubMed:17671168). Localizes in endosome-like structures in
CC ventral cord dendrites. During hypoxia, diffused cytoplasmic
CC localization. Localization in the ventral nerve cord is regulated by
CC egl-9 isoform e and cdk-5 (PubMed:22252129). Co-localizes with rab-6.2
CC in neuronal cell bodies (PubMed:22213799). Co-localizes with rme-8 in
CC puntate structures in neuronal cell bodies and in the intestine
CC (PubMed:22213799). {ECO:0000269|PubMed:10359617,
CC ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22213799,
CC ECO:0000269|PubMed:22252129}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C09H6.2a};
CC IsoId=O17583-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C09H6.2b};
CC IsoId=O17583-2; Sequence=VSP_004305;
CC -!- TISSUE SPECIFICITY: Expressed in vulval epithelial cells and neurons.
CC {ECO:0000269|PubMed:10359617}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC -!- DOMAIN: PDZ protein interaction domains may not be essential for
CC function in vulval induction.
CC -!- PTM: Phosphorylated on multiple Ser and Thr residues by cdk-5 which
CC regulates its localization (PubMed:17671168, PubMed:22252129).
CC {ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22252129}.
CC -!- PTM: May be hydroxylated by egl-9 isoform e on multiple Pro residues
CC which may prevent phosphorylation by cdk-5.
CC {ECO:0000269|PubMed:22252129}.
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DR EMBL; AJ133374; CAB40208.1; -; mRNA.
DR EMBL; BX284601; CAB03869.1; -; Genomic_DNA.
DR EMBL; BX284601; CAC42256.1; -; Genomic_DNA.
DR PIR; T19171; T19171.
DR RefSeq; NP_001020996.1; NM_001025825.3. [O17583-2]
DR RefSeq; NP_492226.2; NM_059825.5. [O17583-1]
DR AlphaFoldDB; O17583; -.
DR SMR; O17583; -.
DR BioGRID; 38031; 22.
DR DIP; DIP-24889N; -.
DR IntAct; O17583; 65.
DR MINT; O17583; -.
DR STRING; 6239.C09H6.2a; -.
DR iPTMnet; O17583; -.
DR EPD; O17583; -.
DR PaxDb; O17583; -.
DR PeptideAtlas; O17583; -.
DR EnsemblMetazoa; C09H6.2a.1; C09H6.2a.1; WBGene00002999. [O17583-1]
DR EnsemblMetazoa; C09H6.2b.1; C09H6.2b.1; WBGene00002999. [O17583-2]
DR GeneID; 172597; -.
DR KEGG; cel:CELE_C09H6.2; -.
DR UCSC; C09H6.2b; c. elegans. [O17583-1]
DR CTD; 172597; -.
DR WormBase; C09H6.2a; CE15610; WBGene00002999; lin-10. [O17583-1]
DR WormBase; C09H6.2b; CE27060; WBGene00002999; lin-10. [O17583-2]
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000171779; -.
DR InParanoid; O17583; -.
DR OMA; EVMHHYF; -.
DR OrthoDB; 393705at2759; -.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR SignaLink; O17583; -.
DR PRO; PR:O17583; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002999; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O17583; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:WormBase.
DR GO; GO:1905852; P:positive regulation of backward locomotion; IMP:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IDA:WormBase.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IDA:WormBase.
DR GO; GO:1902946; P:protein localization to early endosome; IMP:UniProtKB.
DR GO; GO:0097120; P:receptor localization to synapse; IMP:WormBase.
DR GO; GO:0043058; P:regulation of backward locomotion; IGI:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:0050975; P:sensory perception of touch; IMP:WormBase.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Golgi apparatus;
KW Hydroxylation; Membrane; Neurogenesis; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Transport.
FT CHAIN 1..982
FT /note="Protein lin-10"
FT /id="PRO_0000084423"
FT DOMAIN 604..788
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 801..886
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 892..968
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 253..280
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10359617"
FT /id="VSP_004305"
FT MUTAGEN 15
FT /note="S->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-26; A-28; A-87; A-155;
FT A-201; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 16
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-27; A-29; A-88; A-156; A-
FT 202; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 26
FT /note="T->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A28; A-87; A-155;
FT A-201; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 27
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-29; A-88; A-156; A-
FT 202; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 28
FT /note="T->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A26; A-87; A-155;
FT A-201; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 29
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-88; A-156; A-
FT 202; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 87
FT /note="S->A: Loss of cdk-5-mediated regulation of synaptic
FT expression; when associated with A-15; A-26; A28; A-155; A-
FT 201; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 88
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-156; A-
FT 202; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 155
FT /note="S->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-201; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 156
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 202; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 201
FT /note="S->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-155; A-358; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 202
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 156; A-359; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 358
FT /note="T->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-155; A-201; A-424; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 359
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 156; A-202; A-425; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 424
FT /note="T->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-155; A-201; A-358; A-444 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 425
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 156; A-202; A-359; A-445 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 444
FT /note="T->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-155; A-201; A-358; A-424 and A-448."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 445
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 156; A-202; A-359; A-425 and A-449."
FT /evidence="ECO:0000269|PubMed:22252129"
FT MUTAGEN 448
FT /note="S->A: Loss of cdk-5-mediated regulation of synaptic
FT localization; when associated with A-15; A-26; A28; A-87;
FT A-155; A-201; A-358; A-424 and A-444."
FT /evidence="ECO:0000269|PubMed:17671168,
FT ECO:0000269|PubMed:22252129"
FT MUTAGEN 449
FT /note="P->A: Abnormal endosomal localization upon hypoxia
FT treatment; when associated with A-16; A-27; A-29; A-88; A-
FT 156; A-202; A-359; A-425 and A-445."
FT /evidence="ECO:0000269|PubMed:22252129"
SQ SEQUENCE 982 AA; 105243 MW; 9CCCF218C449E96A CRC64;
MSSEAVAQAT AATTSPEHGV PTSSATPTPP PSKGGGAGGG GGGEQQQVPF QMIPPGHFFA
NPFLNPYIPT AGAPAQEGEA QPQMVFSPAQ YQEVMHHYFQ QMMAASGAQF PIPFPMQFQP
ALQQPRPSSQ ASSSHRSEDD NGRQTAGSVV SSNVSPNHRE VRPAEDSTET SGVVQNNDEL
LVPTSTSSDV TIGDVIEKSD SPENSQESAG GEEKSEEKRK LSGDRTDSLI RKQMSEMEKE
ITRRSQNKNI KTIDDDGLAE LIGGSSTRTV ADDFSPFVDK SGLSYTAPAP PSTEKSAPKE
SLNQLRSSFN LPDDSTTVGP VGPSTVPQQS QQFANNSMFM ANAGNFVQNA FPIGVTMTPQ
ATFGAAPGFQ MMQPHQHNLF MQQPNPTFVN NGTNPFLQTQ ATLPNFVQNG TAPLVPTVSA
QQFTPEQLAA AFAQQQIAQS AAPTPFDSPP PSMPSTSSGP SGALAPPPPP SHPIPRRVSG
NGWPEENKEN GTSTSTTNGA QSVPAAAGTD DPVWVLRDSY LKKMQREQRT SEEEEMSWQE
AATAAQEAAE NGGGDDQEEQ ETDRLLNGGT TGASTKGAER RGSVDKKKNS KETMVHEPAV
LIEGVLFRAR YLGSTQMLCE SRGSKAARMA QAQEAVARVK APEGDVQPST EIDLFISTEK
IMVLNTDLQR ISDTDVRQDI LMDHALRTIS YIADIGDLVV LMARRMSTSH SDESCSDGDS
SGGGVRKTPK VICHVFESDE ASFIAQSIGQ AFQVAYVEFL RANGIDDPSY LRQIDYQEVL
NSQELLGDEL EMFAKKETQK EVVVPKKAGE PLGIVVVESG WGSMLPTVVL AHMNPVGPAA
HSNKLNIGDQ IININGISLV GLPLSAAQTQ IKNMKTATAV RMTVVSTPPV VEVRIRRPDT
KYQLGFSVQN GVICSLLRGG IAERGGIRVG HRIIEINGTS VVAVAHDRIV NMLATAVGEI
HMKTMPTSMF RLLTGQEQPQ YI
